Computational studies of H5N1 hemagglutinin binding with SA-alpha-2, 3-Gal and SA-alpha-2, 6-Gal.

Abstract:

:For influenza H5N1 hemagglutinin, a switch from SA-alpha-2, 3-Gal to SA-alpha-2, 6-Gal receptor specificity is a critical step leading to the conversion from avian-to-human to human-to-human infection. Therefore, the understanding of the binding modes of SA-alpha-2, 3-Gal and SA-alpha-2, 6-Gal to H5N1 hemagglutinin will be very important for the examination of possible mutations needed for going from an avian to a human flu virus. Based on the available H5N1 hemagglutinin crystal structure, the binding profiles between H5N1 hemagglutinin and two saccharide ligands, SA-alpha-2, 3-Gal and SA-alpha-2, 6-Gal, were investigated by ab initio quantum mechanics, molecular docking, molecular mechanics, and molecular dynamics simulations. It was found that SA-alpha-2, 3-Gal has strong multiple hydrophobic and hydrogen bond interactions in its trans conformation with H5N1 hemagglutinin, whereas the SA-alpha-2, 6-Gal only shows weak interactions in a different conformation (cis type).

authors

Li M,Wang B

doi

10.1016/j.bbrc.2006.06.179

subject

Has Abstract

pub_date

2006-09-01 00:00:00

pages

662-8

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(06)01431-8

journal_volume

347

pub_type

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